1lta: Difference between revisions

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<StructureSection load='1lta' size='340' side='right'caption='[[1lta]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1lta' size='340' side='right'caption='[[1lta]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1lta]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTA FirstGlance]. <br>
<table><tr><td colspan='2'>[[1lta]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lta OCA], [https://pdbe.org/1lta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lta RCSB], [https://www.ebi.ac.uk/pdbsum/1lta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lta ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lta OCA], [https://pdbe.org/1lta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lta RCSB], [https://www.ebi.ac.uk/pdbsum/1lta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lta ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ELBP_ECOLX ELBP_ECOLX]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. [[https://www.uniprot.org/uniprot/ELAP_ECOLX ELAP_ECOLX]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.  
[https://www.uniprot.org/uniprot/ELBP_ECOLX ELBP_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lta ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lta ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The galactose-binding site in cholera toxin and the closely related heat-labile enterotoxin (LT) from Escherichia coli is an attractive target for the rational design of potential anti-cholera drugs. In this paper we analyse the molecular structure of this binding site as seen in several crystal structures, including that of an LT:galactose complex which we report here at 2.2 A resolution. The binding surface on the free toxin contains several tightly associated water molecules and a relatively flexible loop consisting of residues 51-60 of the B subunit. During receptor binding this loop becomes tightly ordered by forming hydrogen bonds jointly to the GM1 pentasaccharide and to a set of water molecules which stabilize the toxin:receptor complex.
Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT).,Merritt EA, Sixma TK, Kalk KH, van Zanten BA, Hol WG Mol Microbiol. 1994 Aug;13(4):745-53. PMID:7997185<ref>PMID:7997185</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1lta" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hol, W G.J]]
[[Category: Hol WGJ]]
[[Category: Kalk, K H]]
[[Category: Kalk KH]]
[[Category: Merritt, E A]]
[[Category: Merritt EA]]
[[Category: Sixma, T K]]
[[Category: Sixma TK]]
[[Category: Zanten, B A.M Van]]
[[Category: Van Zanten BAM]]
[[Category: Enterotoxin]]
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